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TOMM5 is a single-pass α-helical small Tom subunit of the mitochondrial TOM translocase, not an independent enzyme or transporter.
"encodes the human homolog of the TOM-complex small subunit **Tom5**, a **single-pass α-helical** protein that is part of the mitochondrial **translocase of the outer membrane (TOM) complex**"
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TOMM5 is an accessory structural/regulatory subunit supporting TOM complex stability, organization, and biogenesis around Tom40.
"TOMM5 is best understood as a **structural/regulatory accessory subunit** of a large membrane translocase, contributing to the assembly, stability, and/or mechanistic routing properties of the TOM pore"
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In the human TOM core structure, Tom5 is single-pass α-helical and sits at the periphery of each Tom40 barrel together with Tom6 and Tom7.
"Tom5 (TOMM5) as a **single-pass α‑helical** subunit that **surrounds** the Tom40 β‑barrel together with Tom6 and Tom7"
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The N-terminal segment of Tom40 traverses the channel and interacts with Tom5 at the periphery of the TOM dimer, a site implicated in recruitment of factors for presequence-lacking precursors.
"the **N‑terminal segment of Tom40** traverses the channel and **interacts with Tom5** at the **periphery** of the TOM dimer"
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Yeast ortholog evidence indicates Tom5 associates with the Tom40 precursor at the SAM complex during late TOM assembly, supporting a conserved role in TOM core biogenesis.
"**Tom5 associates with the Tom40 precursor at the SAM complex** in a later stage that promotes Tom40 assembly"